Strikingly Different Localization of Galectin-3 and Galectin-4 in Human Colon Adenocarcinoma T84 Cells

Huflejt, Margaret E.; Jordan, Elizabeth; Gitt, Michael A.; Barondes, Samuel H.; Leffler, Hakon

doi:10.1074/jbc.272.22.14294

Cited by 87 publications

(77 citation statements)

References 41 publications

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“…The apical localization of galectin-3 was previously observed in T84 cells and other polarizing epithelial cell lines (Lindstedt et al 1993;Huflejt et al 1997). Galectin-3 is required for intracellular sorting and correct targeting of glycoproteins to the apical plasma membrane (Delacour et al 2006).…”

Section: Discussionmentioning

confidence: 81%

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

Nio‐Kobayashi

Takahashi-Iwanaga

Iwanaga

2008

J Histochem Cytochem.

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S U M M A R Y Galectin, an animal lectin that recognizes b-galactoside of glycoconjugates, is abundant in the gut. This IHC study showed the subtype-specific localization of galectin in the mouse digestive tract. Mucosal epithelium showed region/cell-specific localization of each galectin subtype. Gastric mucous cells exhibited intense immunoreactions for galectin-2 and galectin-4/6 with a limited localization of galectin-3 at the surface of the gastric mucosa. Electron microscopically, galectin-3 immunoreactivity coated indigenous bacteria on the gastric surface mucous cells. Epithelial cells in the small intestine showed characteristic localizations of galectin-2 and galectin-4/6 in the cytoplasm of goblet cells and the baso-lateral membrane of enterocytes in association with maturation, respectively. Galectin-3 expressed only at the villus tips was concentrated at the myosin-rich terminal web of fully matured enterocytes. Epithelial cells of the large intestine contained intense immunoreactions for galectin-3 and galectin-4/6 but not for galectin-2. The stratified squamous epithelium of the forestomach was immunoreactive for galectin-3 and galectin-7, but the basal layer lacked galectin-3 immunoreactivity. Outside the epithelium, only galectin-1 was localized in the connective tissue, smooth muscles, and neuronal cell bodies. The subtype-specific localization of galectin suggests its important roles in host-pathogen interaction and epithelial homeostasis such as membrane polarization and trafficking in the gut. GALECTIN is a b-galactoside-binding lectin, which to date consists of 15 members (galectin-1 to galectin-15) in mammals and is broadly distributed in a variety of cells and tissues (Leffler et al. 2004). Galectin is likely secreted extracellularly through a non-classical unknown pathway because it lacks a signal sequence essential for insertion into the endoplasmic reticulum (Hughes 1999). Extracellular galectin may mediate cell-cell or cell-matrix adhesion by recognizing cell surface glycoproteins and glycolipids or glycosylated extracellular matrix (Hughes 2001). It also seems capable of regulating cell signaling and membrane trafficking by cross-linking the cell surface receptors (Rabinovich et al. 2007a). A special type of galectin (galectin-3) is involved in host-pathogen interaction through the recognition of a surface carbohydrate of microorganisms (Sato and Nieminen 2004). In contrast, the predominant localization of galectin in the cytoplasm has been frequently observed, suggesting an additional possibility that galectin operates intracellularly to cell proliferation, differentiation, and apoptosis (Hsu and Liu 2004).In the mouse, nine subtypes of galectin (galectin-1, -2, -3, -4, -6, -7, -8, -9, and -12) have been reported to be expressed in a tissue/cell-specific manner. The digestive tract is one of the organs rich in galectin; we previously showed at the mRNA level that at least six subtypes of galectin (galectin-2, -3, -4, -6, -7, and -9) were intensely and continuously expressed from t...

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Section: Discussionmentioning

confidence: 81%

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

Nio‐Kobayashi

Takahashi-Iwanaga

Iwanaga

2008

J Histochem Cytochem.

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“…GaL3 has been shown to induce chemotaxis of monocytes and macrophages at micromolar concentrations. 24 Because GaL3 is known to reach relatively high concentrations in the cytosol of many cell types, 25 of which a high percentage is secreted, 26 such local chemotactic concentrations might be reachable.…”

Section: Discussionmentioning

confidence: 99%

Galectin-3 Gene Inactivation Reduces Atherosclerotic Lesions and Adventitial Inflammation in ApoE-Deficient Mice

Nachtigal

Ghaffar

Mayer

2008

The American Journal of Pathology

116

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This study has examined the role of galectin-3 (GaL3), a multicompartmented N-acetyllactosamine-binding chimeric lectin, on atherogenesis in the ApoE-deficient mouse model of atherosclerosis. Pathological changes consisting of atheromatous plaques, atherosclerotic microaneurysms extending into periaortic vascular channels, and adventitial and periaortic inflammatory infiltrates were assessed in an equal number (n ‫؍‬ 36) of apolipoprotein (Apo)E-deficient mice and ApoE-GaL3 double-knockout mice. These mice were divided into three age groups, 21 to 23 weeks, 25 to 31 weeks, and 36 to 44 weeks of age. Results of this morphological analysis have shown an age-related increase in the incidence of aorta atheromatous plaques and periaortic vascular channels in ApoEdeficient mice. By contrast ApoE/GaL3 double-knockout mice did not show an increase in pathological changes with age. The 36-to 44-week group of ApoE

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“…By its ability to bind to N-lactosamine residues present on the intracellular, extracellular and cell surface associated glycoconjugates, galectin-3 is involved with a number of cellular functions like cell growth, cell adhesion, cell differentiation, tumor progression, angiogenesis and metastasis (Liu et al, 2002;Takenaka et al, 2004;Dumic et al, 2006). Galectin-3 is phosphorylated by casein kinase I in vitro at serine 6 amino acid (Huflejt et al, 1993) and it exists in this phosphorylated form inside the cell (Cowles et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Galectin-3 in apoptosis, a novel therapeutic target

Nangia‐Makker

Nakahara

Hogan

et al. 2007

J Bioenerg Biomembr

112

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During the past decade, extensive progress has been made toward understanding the molecular basis for the regulation of apoptosis. In mammalian cells undergoing apoptosis, two distinct mechanisms or pathways are operated and are triggered by cell death stimuli from intra-or extracellular environments, namely the intrinsic or extrinsic pathways, resulting in mitochondrial membrane depolarization. Several lines of evidence from our laboratories and others have indicated that galectin-3 plays an important role in these pathways by binding to various ligands. Here the authors provide a brief discussion on the role of endogenous or extra-cellular galectin-3 in the regulation of apoptosis and how it could be used as a therapeutic target using natural plant products as its functional inhibitors.

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Strikingly Different Localization of Galectin-3 and Galectin-4 in Human Colon Adenocarcinoma T84 Cells

Cited by 87 publications

References 41 publications

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

Galectin-3 Gene Inactivation Reduces Atherosclerotic Lesions and Adventitial Inflammation in ApoE-Deficient Mice

Galectin-3 in apoptosis, a novel therapeutic target

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